› 4oxi

X-ray diffraction
2.26Å resolution

Crystal structure of Vibrio cholerae adenylation domain AlmE in complex with glycyl-adenosine-5'-phosphate

Released:
DOI: 10.2210/pdb4oxi/pdb
PDB entry 4oxi coloured by chain, front view.
PDB entry 4oxi coloured by chain, side view.
PDB entry 4oxi coloured by chain, top view.
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Primary publication:
Antimicrobial peptide resistance of Vibrio cholerae results from an LPS modification pathway related to nonribosomal peptide synthetases.
Henderson JC, Fage CD, Cannon JR, Brodbelt JS, Keatinge-Clay AT, Trent MS
OpenAccess logo ACS Chem Biol 9 2382-92 (2014)
PMID: 25068415

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192061 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AMP-dependent synthetase/ligase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 576 amino acids
Theoretical weight: 65.37 KDa
Source organism: Vibrio cholerae O1 biovar El Tor str. N16961
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9KRQ7 (Residues: 1-556; Coverage: 100%)
Gene name: VC_1579
Sequence domains: AMP-binding enzyme
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GAP 1 x GAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P3121
Unit cell:
a: 116.039Å b: 116.039Å c: 99.584Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.166 0.193
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

13 review citations

Function and Biogenesis of Lipopolysaccharides.
Bertani et al. (2018)
12 more

2 mentions without citation

Structural advances toward understanding the catalytic activity and conformational dynamics of modular nonribosomal peptide synthetases.
Patel et al. (2023)
1 more